1. Field of the Invention
The present invention relates to a method for increasing thermal stability of recombinant proteins, and more particularly relates to a method of increasing thermal stability of target proteins by fusing self-assembling amphipathic peptides (SAPs) to their N- or C-terminal.
2. Description of the Related Art
Self-assembling amphipathic peptides are a category of peptides that have unique sequences with alternating hydrophobic and hydrophilic residues and can spontaneously assemble into ordered nanostructures. These peptides can increase activity and stability of enzymes through hydrogenation.
To date, a vast number of enzymes isolated from different organisms are widely used in industrial productions. In order to achieve a wider range of applications of industrial enzymes, improving thermal stability of these enzymes is imperative. There were several methods used for improving thermal stability of enzymes, such as: 1) directed molecular evolution, which uses site-directed, random or saturated mutagenesis to look for enzymes with increased thermal stability. This method is depends on the analysis of crystal structure or establishment of a high throughput screening assay. 2) identification and isolation of thermal stability of enzymes from thermophilic microorganisms. However, these methods have limitations and can not be suitable for improving of thermal stability of all the enzymes. There is a need to develop simple and effective methods suitable for increasing thermal stability of a wide spectrum of proteins. The present invention satisfies this need and provides other benefits as well.